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Yoshiki YAMASAKI, Yukio SUZUKI
1980 Volume 44 Issue 4 Pages
707-715
Published: 1980
Released on J-STAGE: November 27, 2008
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Two forms of α-glucosidase were isolated from rice seeds at the milky stage by a procedure that included fractionation with ammonium sulfate, DEAE-cellulose column chromatography, CM-cellulose column chromatography, SP-Sephadex column chromatography and preparative disc gel electrophoresis. The isolated a-glucosidases were designated as α-gluco-sidase I and α-glucosidase II, and were glycoproteins containing 5.5% and 3.4% carbohydrate, respectively. The molecular weight and isoelectric point were: 78900 and pH 9.3 for α-glu-cosidase I, and 47300 and pH 9.3 for α-glucosidase II. They were found to be homogeneous on polyacrylamide disc gel electrophoresis. The two enzymes hydrolyzed maltose, maltotriose, phenyl α-maltoside, amylose and soluble starch to liberate glucose, but did not act on sucrose. Their enzymes produced maltotriose and 4-α-nigerosyl-glucose from maltose as main α-glucosyltransfer products. They hydrolyzed amylose to liberate α-glucose.
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Masayuki SATO, Akira KAJI
1980 Volume 44 Issue 4 Pages
717-721
Published: 1980
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An exopolygalacturonate lyase (EC 4.2.2.9) was purified to a homogeneous state from the culture filtrate of
Streptomyces massasporeus. The molecular weight was estimated to be about 54000 and the isoelectric point was pH 5.5. The enzyme was most active at pH 9.5 and 40°C, and was relatively stable at pH 3.0 to 10.0 (at 2°C for 72 hr) and below 50°C (at pH 7.0 for 10 min). Ca
2+ was required for maximum activity. The enzyme was most active on trigalac-turonic acid and had higher activity on low methoxyl pectins rather than on polygalacturonic acid. The enzyme removed terminal unsaturated digalacturonate units from the galacturonide chains.
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Masako YAMAMOTO, Yuji TADOKORO, Hiroshi IMAI, Kiyo MITA
1980 Volume 44 Issue 4 Pages
723-729
Published: 1980
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Sulfated polysaccharides extracted from
Ulva pertusa (UP) and
Ulva conglobata (UC) were purified on DEAE-cellulose and Sepharose 4B gel columns. Both polymers were confirmed to be homogeneous by gel-filtration chromatography and ultracentrifugation. They were composed of rhamnose, xylose, glucuronic acid, glucose, galactose and sulfate. UP contained a high level of glucuronic acid (27%) and UC, a low level (6%), and galactose was not detected in UP. A sedimentation equilibrium measurement showed distinctly different molecular weights: 9.1×10
4 for UP and 8.2×10
5 for UC, and these results were in good agreement with values estimated by gel chromatography. Specific optical rotations for UP and UC also differed at, [α]
20D=-77.8° and -26.3°, respectively. In spite of these differences, the two polymers showed similar physicochemical behavior and had similar random coil conformation in acidic buffer solutions.
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Shun-ichi TAKEWAKI, Seiya CHIBA, Atsuo KIMURA, Hirokazu MATSUI, Yoshih ...
1980 Volume 44 Issue 4 Pages
731-740
Published: 1980
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Two kinds of a-glucosidase (I and II) were isolated from honey bees by salting-out chromatography with ammonium sulfate. α-Glucosidase I was purified by chromatography on CM-cellulose and gel filtration on. Sephadex G-100. α-Glucosidase II was purified by chromatographies on DEAE- and CM-cellulose and by gel filtration on Bio-Gel P-150. Both enzyme preparations were homogeneous in tests by disc electrophoresis. The molecular weight of α-glucosidases I and II was estimated to be approximately 9.8×10
4 and 7.6×10
4, respectively, by SDS disc electrophoresis. α-Glucosidases I and II were glycoproteins whose carbohydrate moieties were about 25% and 15%, respectively. Their pH optima were 5.0. Both α-glucosidases readily hydro-lyzed phenyl-α-glucoside, sucrose and maltose. α-Glucosidase I showed no activity toward isomaltose and soluble starch, but α-glucosidase II showed relatively high activity toward isomaltose and slight activity toward soluble starch.
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Etsushiro DOI, Daisuke SHIBATA, Teruyoshi MATOBA, Daizo YONEZAWA
1980 Volume 44 Issue 4 Pages
741-747
Published: 1980
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Resting rice seeds contained an acid protease whose optimal pH was 3.5 for casein containing 3.6
M urea and 2.5_??_3.0 for acid denatured haemoglobin. The enzyme was stable in a pH range between 5 and 9. The apparent molecular weight of the enzyme was 60000_??_65000. The enzyme was separated into several fractions by ion-exchange chromatography on DE-32 and by isoelectric focusing. Multiple forms of the enzyme were assumed to be due to the complex formation of the enzyme and inactive proteins. The enzyme activity was completely inhibited by 1×10
-6M pepstatin. ID
50 value of the enzyme for pepstatin was estimated to be 5×10
-8M, which indicates a high affinity of the enzyme for pepstatin. The enzyme is a typical acid protease (carboxyl proteinase) that is sensitive to pepstatin.
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Masakazu HIRASAWA, Goro TAMURA
1980 Volume 44 Issue 4 Pages
749-758
Published: 1980
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A ferredoxin-dependent nitrite reductase from
Spinacea oleracea was purified approximately 180-fold, with a specific activity of 285 units/mg protein. This purified enzyme also had methyl viologen-dependent nitrite reductase activity, with a specific activity of 164 units/mg protein. After disc electrophoresis with polyacrylamide gel, the purified enzyme showed one major and one minor protein band.
The molecular weight of the enzyme was estimated to be 86000 from Ultrogel filtration. This purified enzyme in oxidized form had absorption peaks at 278, 390, 573 and 690nm. The absorbance ratios, A
390: A
278 and A
573: A
390 were 0.61 and 0.37, respectively.
By applying the purified enzyme to DEAE-Sephadex A-50 column chromatography, the ferredoxin-dependent nitrite reductase activity was selectively decreased. However, the methyl viologen-dependent nitrite reductase activity was increased, with a specific activity of 391 units/mg protein. This modified enzyme was homogeneous by disc electrophoresis with polyacrylamide gel.
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Teruhiko BEPPU, Katsuya GOMI, Dalel Singh DAHIYA, Shigeru HOSHIKO, Kei ...
1980 Volume 44 Issue 4 Pages
759-764
Published: 1980
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Microorganisms utilizing
erythro-L
S isocitrate (L-alloisocitrate) were isolated from soil after enrichment culture in medium containing the acid as the sole carbon source. Most isolates were bacteria, and NAD
+-linked L-alloisocitrate dehydrogenase activity was found in some of their cell-free extracts. A bacterial strain No. 2 showing the highest enzyme activity was identified as belonging to genus
Pseudomonas. A fungal strain showing good growth on L-alloisocitrate but restricted growth on glucose was also isolated and identified as belonging to genus
Acremonium. No dehydrogenase nor oxidase activity was detected for L-alloisocitrate in extracts of the fungus, although conversion of the acid to fumarate was suggested in tracer
experiments with intact cells.
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Tetsu ANDO, Ken-ichi KISHINO, Sadahiro TATSUKI, Nobutaka TAKAHASHI
1980 Volume 44 Issue 4 Pages
765-775
Published: 1980
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The sex pheromone of the rice green caterpillar,
Naranga aenescens Moor, was presumed to be a mixture of some unsaturated acetates using electroantennogram technique. Abdominal tips of virgin females were shown to contain (
Z)-9-tetradecenyl acetate (compound I), (
Z)-9-hexadecenyl acetate (compound 11) and (
Z)-11-hexadecenyl acetate (compound III) in a ratio of 1:1:4, respectively. These synthetic three compounds were individually active on the male antenna but only the mixture of the three compounds attracted the male moths in a field. Field traps containing the three compounds in a ratio of 1:1:4 (1mg/rubber septum) consistently attracted more males than traps baited with two unmated females.
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Hiroyuki HORITSU, Haruyasu KATO
1980 Volume 44 Issue 4 Pages
777-782
Published: 1980
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A cadmium-sensitive mutant strain was isolated from a Cd
2+-tolerant bacterium,
Pseudomonas aeruginosa G-1 strain by mutagenesis with
N-methyl-
N'-nitro-
N-nitrosoguanidine. The Cd
2+-sensitive mutant strain was about 8-times as sensitive to Cd
2+ and 2-times as sensitive to Hg
2+, Cr
2+ and achromycin, and not sensitive to Cu
2+, as the parent strain.
Vacuole-like substances were observed in the parent strain by transmission electron microscope in the presence of Cd
2+, but not in the absence of Cd
2+. The mutant strain took up 3.3-times the amount of Cd
2+ into cells when compared with the parent strain. Disc electrophoretic patterns showed a characteristic protein band in the parent strain at the stationary phase, but the corresponding protein band was present in the mutant strain at the late exponen-tial phase.
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Hideyuki MATSUDA, Kohkichi MORITA, Osamu HIRAYAMA
1980 Volume 44 Issue 4 Pages
783-790
Published: 1980
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A lipolytic acyl-hydrolase purified from
Phaseolus vulgaris catalyzed the hydrolysis of fatty acid ester bonds at both C-1 and C-2 positions of the glycerol of monogalactolipid and phosphatidylcholine, and the corresponding lysolipids were not detected in the reaction mixture. When methanol was added to the reaction mixture, fatty acid methyl esters were obtained in the products. These results suggest that the enzyme not only has activity to completely deacylate both galacto- and phospholipids but also has acyl transferase activity.
A competitive relation was found between monogalactosyldiacylglycerol and phosphatidylcholine as substrates of the enzyme, indicating that the active sites toward both substrates are the same.
The chemical modification suggested that histidine and tryptophan residues are important to the enzymic activities.
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Toshiyuki WATANABE, Keitaro TAKAHASHI, Kazuo MATSUDA
1980 Volume 44 Issue 4 Pages
791-797
Published: 1980
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Treatment of xyloglucan from jojoba seeds with purified cellulase from
Trichoderma viride, followed by gel filtration on Bio-Gel P-2, yielded higher and lower oligosaccharide fractions. From the latter fraction, six kinds of pure oligosaccharides were obtained by preparative paper chromatography. Examination of the partial acid hydrolyzates of the oligosaccharides, the molar ratio of the component monosaccharides, treatment with partially purified β-glucosidase from
Aspergillus oryzae enzyme preparation and the degree of polymeriza-tion by gel filtration on Bio-Gel P-2 showed them to be: (a) isoprimeverose; (b)_??_.
View full abstract
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Kazuo AISAKA, Osamu TERADA
1980 Volume 44 Issue 4 Pages
799-805
Published: 1980
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Lipoprotein lipase (LPL) and lipase activities from
Rhizopus japonicus KY 521 were separated into two peaks by Sephadex G-100 gel filtration. Peak I (LPL) with higher LPL activity than lipase activity was further purified by chromatography on hydroxylapatite, gel filtration on Sephadex G-150 and isoelectric focusing. The purified enzyme had LPL activity and lipase activity in a ratio of 1.5:1. The two activities showed similar catalytic properties; they could hydrolyzed tricaprin most rapidly among triglycerides tested, had an optimum pH around 8.3 and were stable in the pH range of 5 to 7 and up to 50°C with treatment for 15 min. However, the LPL activity of the purified enzyme was strongly inhibited by NaCl and protamine, whereas lipase activity was enhanced by them.
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Yoshiaki NOMA
1980 Volume 44 Issue 4 Pages
807-812
Published: 1980
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Many actinomycetes, newly isolated from soil, converted (-)-carvone to either (-)-
trans-carveol or (-)-
cis-carveol or to a mixture of both compounds, and known metabolic products, such as (+)-dihydrocarvone, (+)-isodihydrocarvone, (+)-neodihydrocarveol, (-)-dihydro-carveol, (+)-isodihydrocarveol and (+)-neoisodihydrocarveol.
Identification of the metabolic products and the metabolic pathways of (-)-carvone were described in a strain of
Streptomyces,
A-
5-
1 and a strain of
Nocardia,
1-
3-
11. A summary shows the reaction mechanism pattern of (-)-carvone conversion by actinomycetes.
View full abstract
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Hiroshi DOI, Bong Sun PARK, Fumio IBUKI, Masao KANAMORI
1980 Volume 44 Issue 4 Pages
813-820
Published: 1980
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The heterogeneity and chemical composition were investigated in
k-casein from colostrum. The acid casein was obtained from four different Holstein cow colostra. The yield of acid casein from colostrum was higher than that from normal milk.
k-Casein from colostrum was prepared by the gel filtration method of Yaguchi
et al. The gel filtration profiles differed among the four colostrum acid caseins.
Colostrum
k-casein was fractionated on a DEAE-cellulose column into one nonadsorbed and six adsorbed fractions with increasing salt concentration. Six adsorbed fractions had the same molecular weight and stabilizing ability for α
s1 -casein in the presence of calcium ion. The amino acid composition and the phosphorus content of the adsorbed fractions were iden-tical, but fractions eluted with high salt concentrations had more carbohydrates (galactose, sialic acid, glucosamine, galactosamine). Colostrum
k-casein was characterized by a higher content of carbohydrate moiety in comparison with normal
k-casein. Also glucosamine which has not been found in normal
k-casein was detected in colostrum K-casein. The
k-casein com-ponent from colostrum contained at least one molecule of carbohydrate, though the carbo-hydrate-free component was detected in normal
k-casein.
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Koichi KATO, Kenji KAWAHARA, Takeshi TAKAHASHI, Seizi IGARASI
1980 Volume 44 Issue 4 Pages
821-825
Published: 1980
Released on J-STAGE: November 27, 2008
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Whole cells of
Xanthomonas citri K24, a penicillinase-deficient α-amino acid ester hydrolase producer, were effectively used for synthesis of amoxicillin from D-α-(
p-hydroxyphenyl)-glycine methyl ester (HPGME) and 6-aminopenicillanic acid (6-APA). The yield of amoxicillin from 6-APA was increased by reducing the ionic strength of the reaction mixture and by ad-ding 2-butanol to the reaction mixture. Increasing the HPGME/6-APA ratio above 1:1 raised the yield of amoxicillin. The optimum pH for the synthetic reaction was between 6 and 7, and the optimum temperature, 20°C. The addition of 2-butanol repressed the enzymatic hydrolysis of HPGME, and enhanced the acylation of 6-APA. More than 90% of the added 6-APA was converted into amoxicillin under the optimum conditions.
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Jihn Sang KIM, Kazutoshi ITO, Hajime TAKAHASHI
1980 Volume 44 Issue 4 Pages
827-833
Published: 1980
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Cells of
Rhodopseudomonas palustris released a large amount of molecular hydrogen when illuminated anaerobically in the presence of certain organic compounds, as electron donors. This hydrogen formation, like nitrogenase activity, was dependent on light illumination. Both hydrogen evolution and nitrogenase activity were almost completely inhibited by addition of ammonium salts. The rate of hydrogen production was almost proportional to nitroogenase activity but no relationship was seen between hydrogen production and hydrogenase activity. In molybdenum starved cells, hydrogen evolution and nitrogenase activity decreased similarly and markedly. Nifmutant strains, which lack nitrogenase activity, were incapable of producing hydrogen. These results suggest that hydrogen production is clearly catalyzed by nitrogenase in this bacterium.
When nitrogen gas or glutamate was used as an inducer for nitrogenase synthesis, lactate was the best substrate for hydrogen evolution among organic acids examined. The rate of hydrogen production with lactate was 40_??_50μl/hr/mg cells (dry weight).
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Takashi TSUGITA, Tadao KURATA, Hiromichi KATO
1980 Volume 44 Issue 4 Pages
835-840
Published: 1980
Released on J-STAGE: November 27, 2008
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Four kinds of rice milled to different degrees (92, 85, 75 and 50% milled rice) were subjected after cooking to odor evaluation tests and to GC and GC-MS analyses by use of the Tenax GC trap and injection techniques. Forty volatile compounds were identified in cooked rice, and there were remarkable differences in both the odor of cooked rice and in the quantity of volatile components between 92 % milled rice and the other three degree of milling. The correspondence in odor evaluation tests and GC quantitative analysis suggests that the surface layer constitutents of the rice grain have an important role in the formation of the odor of cooked rice.
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Shiro YAMASHOJI, Hiromi YOSHIDA, Goro KAJIMOTO
1980 Volume 44 Issue 4 Pages
841-847
Published: 1980
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The effects of His and Cu (II)-His complex were examined on photosensitized oxidation of linoleic acid (LA) in the FMN (riboflavin 5'-phosphate)-light system. The generation of superoxide anion (0
2-) and the peroxidation of LA were promoted by addition of His, and they were inhibited by addition of Cu (II)-His complex. The peroxidation of LA by 0
2-resulted in the formation of H
2O
2 and linoleic acid hydroperoxide (LAHPO). Cu(II)-His complex promoted the decomposition of H
20
2 and LAHPO during generation of 0
2-, and the decomposition of H
20
2 by the complex resulted in limited OH formation. Cu (II)-His complex inhibited both oxygen uptake and the accumulation of peroxides, and the decreases in both were similar. These results suggest that the antioxidant activity of Cu(II)-His complex may be attributed to the quenching of 0
2- rather than to catalytic action on decomposition of peroxides.
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Yoshiki TANI, Motohiro MATSUURA, Takaharu NEGORO, Hideaki YAMADA
1980 Volume 44 Issue 4 Pages
849-854
Published: 1980
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A paper disc assay method was developed that detect a compound which might function as a biosynthetic intermediate of vitamin B6 (B6). The amounts of total B6-vitamers and true B6 were determined by growth responses to a B6-requiring mutant of
Esherichia coli B and
Saccharomyces carlsbergensis, respectively. The difference between the amounts of total and true B6 was calculated as the amount of biosynthetic intermediates of B6. Screening for intermediate activity was carried out among culture broths of over one thousand strains of actinomycetes. A B6-vitamer was isolated from the culture broth of an actinomycete and identified as alanine. n-Cysteine, L-cysteine, L-cystine and β-hydroxypyruvate were also estimated to be such compounds after the screening in various kinds of compounds. The B6-vitamer activities of these amino acids were discussed.
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Yasuhiro KOJIMA, Natsuki KATO
1980 Volume 44 Issue 4 Pages
855-862
Published: 1980
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A new synthetic route to perhydrofuro [2, 3-b] furan was developed by employing 3-sub-stituted furan derivatives (
t-butyl and phenyl systems) that were derived by coupling reaction with epoxides and a new reagent, lithium di (3-furyl) cuprate. The synthesized furo-furan compounds were prepared to various derivatives for testing antifeeding activities. The results suggest that higher degree activities depend on the presence of a moderately polar, substituent group. Moreover, in order to enhance the antifeeding activities, the hydroxy group of the hem iacetal should be protected with an acyl or methyl group.
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Hiromichi OHTA, Hatsuki TETSUKAWA
1980 Volume 44 Issue 4 Pages
863-867
Published: 1980
Released on J-STAGE: November 27, 2008
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Esters of secondary alcohols were enantioselectively hydrolyzed with
Brevibacterium ammoniagenes IAM 1645, ATCC 6872 to give the corresponding chiral alcohols and esters. While the esters of alkyl vinyl carbinols gave (
S)-alcohols, dialkyl carbinol esters were hydrolyzed to (
R)-alcohols of rather low optical purities. Hydrolysis of α-phenethyl acetate proceeded smoothly resulting in the formation of (
R)-α-phenethyl alcohol in good optical yield. The structure of the acyl moiety of 1-tridecen-3-yl esters seriously influenced the rate and optical yield of the reaction, and the acetate was found to give the best results.
View full abstract
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Kenji WATANABE, Shigeshi TAKESUE, Kazuko ISHIBASHI, Shunsuke NAKAHARA
1980 Volume 44 Issue 4 Pages
869-875
Published: 1980
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A kinetic model representing PL-1 phage adsorption to host bacterium
Lactobacillus casei ATCC 27092 was simulated by using a digital computer. By trial and error process, equation (I) agreed closely with the experimental results, and the approximate values of the parameter, rate constant, were calculated to be:
k1B=0.19,
k2=0.04,
k3=0.04 and
k4B=0.04 (1/ml).
Reversible complex (b)_??_Free phage_??_Reversible complex (a)_??_Irreversible complex
(1) In this case, however, for a best fit it was necessary to make an additional assumption that the phage population contained a small proportion of slowly-adsorbing phages and to make some corrections for
k1 and
k4 after the relative amount of free phage against input phage taken as 1.0 decreased below 0.1. The existence of such heterogeneous phages was confirmed experimentally. The significance of the parameter in the process of PL-1 phage adsorption was discussed.
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Munekazu TAGAWA, Hideo YAMAGATA, Shigezo UDAKA
1980 Volume 44 Issue 4 Pages
877-882
Published: 1980
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The genetic background of the protein-leaky mutant of
Escherichia coli (PE4LA) was examined. This mutant preferentially excretes periplasmic proteins and outer membrane components. The results obtained from various crosses indicated that the mutation responsible for protein leakage was located near the
purE gene. The amount of protein excreted decreased to about half whenever PE4LA was converted from Pur
- to Pur
+ either by transduction or spontaneous reversion. When purine or pyrimidine auxotrophs were obtained from
purE+ revertant of PE4LA, only auxotrophs whose blockages were located at a step identical or close to that governed by
purE gene excreted proteins to the same extent as PE4LA. Excess adenine in the culture medium repressed exprotein accumulation by PE4LA. These results suggest that
purE is involved in some way with protein excretion, and perhaps the accumulating metabolic intermediate(s) causes protein excretion due to a defect in
purE enzyme.
View full abstract
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Junji MORITA, Naoki KASHIMURA, Tohru KOMANO
1980 Volume 44 Issue 4 Pages
883-890
Published: 1980
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The inactivation of bacteriophage φX174 by D-fructose 6-phosphate was investigated. This inactivation was inhibited by EDTA or reducing agents, and stimulated by Cu
2+ but other metal ions could not be substituted for Cu
2+. The reaction was also inhibited by superoxide dismutase (EC 1.15.1.1), catalase (EC 1.11.1.6) and various free radical scavengers.
No detectable changes were observed in adsorption capacity of phage and in the conformation of the virion. The viral DNA in the virion was, however, found to be cleaved. This strand scission was also enhanced by Cu
2+ and protected by catalase. Similar results were obtained when φX174 DNA was directly treated with D-fructose 6-phosphate.
It is concluded that the inactivation of φX174 is due to DNA strand scission in the virion by the free radical of D-fructose 6-phosphate or oxygen radicals generated during autoxidation of D-fructose 6-phosphate.
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Rikimaru HAYASHI, Ikuko KAMEDA
1980 Volume 44 Issue 4 Pages
891-895
Published: 1980
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The tritium-hydrogen exchange method was used to determine the total racemization of amino acid residues of four proteins (ribonuclease A, lysozyme, soybean protein and casein) during their exposure to an alkali. Tritium was incorporated with first order kinetics into these proteins during their incubation in 0.2
N NaOH at 40°C. The tritium-hydrogen exchange increased as the temperature and the alkali concentration increased. In contrast, pepsin digestibility decreased extensively in the initial stage of the treatment. This phenomenon was verified by the subsite theory of protease, that only minor racemization renders the extended range of the peptide chain around the racemized amino acids non-susceptible to pepsin. General precautions against the racemization of food protein treated with alkalis are discussed briefly in terms of the deterioration of nutrients.
View full abstract
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Takeshi KITAHARA, Yoshikazu TAKAGI, Masanao MATSUI
1980 Volume 44 Issue 4 Pages
897-901
Published: 1980
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Two novel minor components isolated from yudzu peel oil were characterized as monoterpene β-ketols,
1 and
3, by their synthesis, and they were converted to related monoterpenes, dihydroneroloxide (
9) neroloxide (
10) and ho-trienol (
11).
View full abstract
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Kazuyoshi KAWAZU, Yoshiki NISHII, Shuhei NAKAJIMA
1980 Volume 44 Issue 4 Pages
903-906
Published: 1980
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Guided by the bioassay with
Bursaphelenchus lignicolus described in the preceding paper, two nematicidal substances were isolated from roots of
Cirsium japonicum and identified with tridec-l-ene-3, 5, 7, 9, 11-pentayne and 9, 10-epoxy-heptadec-l6-ene-4, 6-diyn-8-ol. These two compounds completely inhibited propagation of the nematode at a dose of 16μg and 250μg, respectively. 1-Phenylhepta-1, 3, 5-triyne and 2-phenyl-5-(1'-propynyl)-thiophene (from
Coreopsis lanceolata) and
cis-dehydromatricaria ester (from
Solidago altissima) also inhibited the propagation at a dose of 110μg.
View full abstract
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Synthesis of Optically Active Cyclopentanes from Carbohydrate
Hiroshi OHRUI, Hiroyoshi KUZUHARA
1980 Volume 44 Issue 4 Pages
907-912
Published: 1980
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Optically active trisubstituted and tetrasubstituted cyclopentanes, with proper functional groups of proper stereochemistry as precursors for chiral synthesis of brefeldin A and prostaglandins, were prepared stereoselectively from carbohydrate.
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Gen-ichi DANNO, Masato NATAKE
1980 Volume 44 Issue 4 Pages
913-918
Published: 1980
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Foxtail millet (
Setaria italica) proteins were fractionated into five fractions,
i.e., water-, salt-, ethanol-, sodium dodecyl sulfate (SDS)- and 2-mercaptoethanol (ME)-soluble fractions, by successive extraction with various solvents from millet flour. The proportion in each fraction was 7.2, 5.6, 40, 25 and 20% respectively, of total flour nitrogen. The proteins of the ethanol- and SDS-soluble proteins were similar in amino acid composition and molecular weight distribution. More than 15 different molecular weight classes of proteins ranging from 11000 to 150000 were distinguished by SDS-polyacrylamide gel electrophoresis without prior reduction of their disulfide bonds. These major protein bands in the gel were estimated to be homo-olygomers (monomer, dimer, trimer, etc.) of subunit A or subunit B. The molecular weights of subunits A and B were 12000 and 17000, respectively. Subunits A and B were also different in amino acid composition: subunit A had higher content of methionine.
View full abstract
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Ikuo MATSUI, Sigeo MURAKAWA, Takeshi TAKAHASHI
1980 Volume 44 Issue 4 Pages
919-920
Published: 1980
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Etsushiro DOI, Nobuhiko KOMORI, Teruyoshi MATOBA, Yuhei MORITA
1980 Volume 44 Issue 4 Pages
921-922
Published: 1980
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Etsushiro DOI, Daisuke SHIBATA, Teruyoshi MATOBA, Daizo YONEZAWA
1980 Volume 44 Issue 4 Pages
923-924
Published: 1980
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Goro TAMURA, Matsuyo KANKI, Masakazu HIRASAWA, Michiei OTO
1980 Volume 44 Issue 4 Pages
925-927
Published: 1980
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Yoshihiro KANAMARU, Ryoya NIKI, Shunrokuro ARIMA
1980 Volume 44 Issue 4 Pages
929-930
Published: 1980
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Hisanao TAKEUCHI, Megumi MAEDA, Yukio YAMAGUCHI, Keiichiro MURAMATSU
1980 Volume 44 Issue 4 Pages
931-935
Published: 1980
Released on J-STAGE: November 27, 2008
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Yoshihiro KOMIYAMA, Mamoru HARAKAWA, Masao TSUJI
1980 Volume 44 Issue 4 Pages
937-939
Published: 1980
Released on J-STAGE: November 27, 2008
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Hideo HAYASHI, Koichi KOSHIMIZU
1980 Volume 44 Issue 4 Pages
941-942
Published: 1980
Released on J-STAGE: November 27, 2008
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Yasuo ARIYOSHI
1980 Volume 44 Issue 4 Pages
943-945
Published: 1980
Released on J-STAGE: November 27, 2008
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Tsutomu MASUDA, Kunio YAMANE, Hideo HIROKAWA, Teruo TANAKA, Kenji SAKA ...
1980 Volume 44 Issue 4 Pages
947-948
Published: 1980
Released on J-STAGE: November 27, 2008
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Takumi KAWAGISHI, Naomichi NISHIO, Ryuichi MATSUNO, Tadashi KAMIKUBO
1980 Volume 44 Issue 4 Pages
949-950
Published: 1980
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Yukiharu SATO, Masao HASEGAWA, Noriko SUTO
1980 Volume 44 Issue 4 Pages
951-952
Published: 1980
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Zensuke MAKI, Misao TASHIRO, Nobuo SUGIHARA, Masao KANAMORI
1980 Volume 44 Issue 4 Pages
953-955
Published: 1980
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Tomoyuki TSUNEYA, Masakazu ISHIHARA, Haruyasu SHIOTA, Minoru SHIGA
1980 Volume 44 Issue 4 Pages
957-958
Published: 1980
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Tsutomu YAMAGUCHI, Yukiko YAMASHITA, Toshio ABE
1980 Volume 44 Issue 4 Pages
959-961
Published: 1980
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Shigehiro HIRANO, Yuji YAGI
1980 Volume 44 Issue 4 Pages
963-964
Published: 1980
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Masayoshi TAKAKUWA, Youichi TAMAI
1980 Volume 44 Issue 4 Pages
965-966
Published: 1980
Released on J-STAGE: November 27, 2008
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Takashi MATSUMOTO, Tsutomu IKEDA, Naomi KANNO, Takuro KISAKI, Masao NO ...
1980 Volume 44 Issue 4 Pages
967-969
Published: 1980
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